Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G
Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G
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DOI：
10.1002/j.1460-2075.1996.tb01108.x
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发表时间：
1996-12-16
期刊：
影响因子：
11.4
通讯作者：
Sachs, AB
中科院分区：
文献类型：
--
作者：
Tarun, SZ;Sachs, AB
尽管帽结构和poly（A）尾位于mRNA分子的相对两端，但先前的工作表明它们相互作用以增强翻译并抑制mRNA降解。在这里，我们提出的生物化学数据表明，结合到mRNA帽（eIF-4F）和聚（A）尾（Pab 1 p）的蛋白质是物理相关的酵母酿酒酵母提取物。具体来说，我们发现Pab 1 p共纯化和免疫沉淀与eIF-4F的eIF-4G亚基。重组酵母eIF-4G蛋白Tif 4632 p上的Pab 1 p结合位点被定位到紧邻其eIF-4 E结合位点的114个氨基酸的区域。Pab 1 p只有在与poly（A）复合时才与该区域结合。这些数据支持mRNA上的Pab 1 p-poly（A）尾复合物可以通过eIF-4G与帽结构相互作用的模型。
Although the cap structure and the poly(A) tail are on opposite ends of the mRNA molecule, previous work has suggested that they interact to enhance translation and inhibit mRNA degradation. Here we present biochemical data that show that the proteins bound to the mRNA cap (eIF-4F) and poly(A) tail (Pab1p) are physically associated in extracts from the yeast Saccharomyces cerevisiae. Specifically, we find that Pab1p co-purifies and to-immunoprecipitates with the eIF-4G subunit of eIF-4F. The Pab1p binding site on the recombinant yeast eIF-4G protein Tif4632p was mapped to a 114-amino-acid region just proximal to its eIF-4E binding site. Pab1p only bound to this region when complexed to poly(A). These data support the model that the Pab1p-poly(A) tail complex on mRNA can interact with the cap structure via eIF-4G.